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Plant Physiology 91:34-38 (1989)
© 1989 American Society of Plant Biologists

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Membranes and Bioenergetics

Purification of an H+-Translocating Inorganic Pyrophosphatase from Vacuole Membranes of Red Beet 1

Vahé Sarafian and Ronald J. Poole

Department of Biology, McGill University, Montréal, P.Q., Canada H3A 1B1

An H+-translocating inorganic pyrophosphatase (PPase) was isolated and purified from red beet (Beta vulgaris L.) tonoplast. One major polypeptide of molecular weight 67 kilodalton copurified with fluoride-inhibitable PPase activity when subjected to one-dimensional polyacrylamide gel electrophoresis. Overall, a 150-fold purification of the PPase was obtained, from the tonoplast fraction, through anion exchange chromatography of the detergent-solubilized membranes followed by ammonium sulfate precipitation and gel filtration chromatography. The purified polypeptide showed no cross-reactivity with antibodies raised against the 67 kilodalton subunit of the tonoplast ATPase.

1 Supported by the Natural Sciences and Engineering Research Council of Canada and the Fonds pour la Formation de Chercheurs et l'Aide à la Recherche of Quebec.






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